ProGP115 (Flavastacin (P40))
Home -> ProGPdb -> Search ProGP -> Display data
ProGP ID | ProGP115 (Flavastacin (P40)) |
Validation Status | Characterized |
Organism Information | |
Organism Name | Flavobacterium meningosepticum (Elizabethkingia meningoseptica) |
Domain | Bacteria |
Classification | Phylum : Bacteroidetes Class : Bacteroidetes Subclass : Flavobacteriia Orders : Flavobacteriales Family : Weeksellaceae Genus : Flavobacterium Species : meningosepticum |
Taxonomic ID (NCBI) | 238 |
Genome Information | |
GenBank | L37784 |
EMBL | L37784 |
Protein Information | |
Protein Name | Flavastacin (P40) |
UniProtKB/SwissProt ID | Q47899 |
EMBL-CDS | AAC41455.1 |
UniProtKB Sequence | >sp|Q47899|FLVS_FLAME Flavastacin OS=Flavobacterium meningosepticum PE=1 SV=1 MTRKLLILSGCLILALNSCKSDMETTPASSVDHTTTQLNGTTIHKLLINGAYTYVNEVNG EYFYADDITITAEQFNQLKRMANPDISTVERSTIVSSFIKTWPNATVYYTLPSQGSLSTQ AYNTFLTNINKAFDMISSKTSVKFVQRTNQTEYITFTYSTGNSSPLGWVKNRVNGIKIYN TTYPAIIAHEIMHSMGIMHEQCRPDRDQYIIVDTNRAQDGTRHNFNLYNDYAGHGEFDFG SVMMYKSTDFAIDPNLPVMTKLDGSTFGKQRDGLSAGDYAGINHLYGPVNSTSATNGTYT LTTSLAGDKNIDITGSSTADGTDVILYSATTGNNQKFIFRKSEHGYFTIKSILDSTKVLT VRNNGTANGTAVELRTNADTDAQKWLLFNLGNEGFGFAPKNAPSLRLEVKDGLTTNLTPI VIGSTDQTLQPYTKQRFTLTKVN |
Sequence length | 443 AA |
Subcellular Location | Periplasm |
Function | Zinc metalloendopeptidase (Zinc-aspartyl endoprotease) of astacin family that cleaves peptides on the amino-terminal side of aspartic acid. EC= 3.4.24.76., these enzymes are involved in extracellular matrix formation, morphogenesis and digestion. |
Glycosylation Status | |
Glycosylation Type | O- (Ser) linked |
Experimentally Validated Glycosite(s) in Full Length Protein | (Signal peptide: 1-15, propeptide: 15-91) S355 |
Experimentally Validated Glycosite(s ) in Mature Protein | S264 |
Glycosite(s) Annotated Protein Sequence | >sp|Q47899|FLVS_FLAME Flavastacin OS=Flavobacterium meningosepticum PE=1 SV=1 MTRKLLILSGCLILALNSCKSDMETTPASSVDHTTTQLNGTTIHKLLINGAYTYVNEVNG EYFYADDITITAEQFNQLKRMANPDISTVERSTIVSSFIKTWPNATVYYTLPSQGSLSTQ AYNTFLTNINKAFDMISSKTSVKFVQRTNQTEYITFTYSTGNSSPLGWVKNRVNGIKIYN TTYPAIIAHEIMHSMGIMHEQCRPDRDQYIIVDTNRAQDGTRHNFNLYNDYAGHGEFDFG SVMMYKSTDFAIDPNLPVMTKLDGSTFGKQRDGLSAGDYAGINHLYGPVNSTSATNGTYT LTTSLAGDKNIDITGSSTADGTDVILYSATTGNNQKFIFRKSEHGYFTIKSILDS*(355)TKVLT VRNNGTANGTAVELRTNADTDAQKWLLFNLGNEGFGFAPKNAPSLRLEVKDGLTTNLTPI VIGSTDQTLQPYTKQRFTLTKVN |
Sequence Around Glycosites (21 AA) | GYFTIKSILDSTKVLTVRNNG |
Technique(s) used for Glycosylation Detection | Phenol-sulfuric acid assay |
Technique(s) used for Glycosylated Residue(s) Detection | Collision activated dissociation (CAD) mass spectrometry and Edman degradation |
Protein Glycosylation- Implication | Glycosylation may contribute towards protein stability |
Glycan Information | |
Glycan Annotation | Linkage: Man- Ser. Branched acidic, heptasaccharide (1244 Da) containing 3 different uronyl analogs, a methylated Rham and Man, a Glc, and a reducing terminal Man. Only pyranose ring forms were detected [(2-OMe)Man1-4GlcNAcU1-4GlcU1-4Glc1-4(2-OMe)GlcU-4[(2-OMe)Rham1-2]Man]. |
BCSDB ID | 137520 |
Technique(s) used for Glycan Identification | ESI-MS (electrospray ionization mass spectrometry), CID (collision-induced dissociation), and a combination of isotopic labeling, composition and methylation analysis. |
Protein Glycosylation linked (PGL) gene(s) | |
Additional Comment | Flavastacin is the first example of a prokaryotic enzyme related to the eukaryotic astacin group. Identified glycosylation Sequon features: Consensus sequon observed Asp-Ser (DS) or Asp-Thr-Thr (DTT), at turns. DT alone may not serve as a sequon. Interestingly, the experimentally examined other five nonglycosylated DT sequons were followed by N, D and Q. |
Literature | |
Year of Identification | 1995 |
Year of Identification Month Wise | 1995.06.02 |
Year of Validation | 1995 |
Reference | Plummer, T.H., Tarentino, A.L. and Hauer, C.R., 1995. Novel, Specific O-Glycosylation of Secreted Flavobacterium meningosepticum Proteins.: Asp-Ser∗ AND Asp-Thr∗-Thr CONSENSUS SITES∗. Journal of Biological Chemistry, 270(22), pp.13192-13196. |
Corresponding Author | Thomas H Plummer Jr |
Contact | Division of Molecular Medicine, Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany 12201-0509, USA. |
Reference | Reinhold, B.B., Hauer, C.R., Plummer, T.H. and Reinhold, V.N. (1995) Detailed structural analysis of a novel, specific O-linked glycan from the prokaryote Flavobacterium meningosepticum. J Biol Chem, 270, 13197-13203. [PubMed: 7768917] |
Corresponding Author | Vernon N Reinhold |
Contact | Department of Immunology Boston University Medical Center 80 East Concord ST Boston |
Reference | Tarentino, A.L., Quinones, G., Grimwood, B.G., Hauer, C.R. and Plummer, T.H., 1995. Molecular cloning and sequence analysis of flavastacin: an O-glycosylated prokaryotic zinc metalloendopeptidase. Archives of biochemistry and biophysics, 319(1), pp.281-285. |
Corresponding Author | Thomas H Plummer Jr A L Tarentino |
Contact | Division of Molecular Medicine, Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany 12201-0509, USA. |